[NMR paper] 31P and 13C solid-state NMR analysis of morphological changes of phospholipid bilayers containing glucagon during fibril formation of glucagon under neutral condition.
31P and 13C solid-state NMR analysis of morphological changes of phospholipid bilayers containing glucagon during fibril formation of glucagon under neutral condition.
Related Articles31P and 13C solid-state NMR analysis of morphological changes of phospholipid bilayers containing glucagon during fibril formation of glucagon under neutral condition.
Authors: Haya K, Makino Y, Kikuchi-Kinoshita A, Kawamura I, Naito A
Abstract
Glucagon is a 29 amino acid peptide hormone secreted by pancreatic ?-cells that interacts with specific receptors located in various organs. Glucagon tends to form gel-like fibrillar aggregates that are cytotoxic due to their activation of apoptotic signaling pathways. To understand the glucagon-membrane interactions, morphological changes in dimyristoylphosphatidylcholine (DMPC) bilayers containing glucagon in neutral solution were investigated by observing 31P NMR spectra. First, lipid bilayers with a DMPC/glucagon molar ratio of 50/1 were observed. One day after preparing the DMPC/glucagon lipid bilayer sample, lipid bilayers were disrupted below the phase transition temperature (Tc). Membrane disruption was reduced 2*days after preparation due to the reduction of glucagon-DMPC interaction, and subsequently increased by 4*days and was reduced again by 7*days. TEM measurements showed that small ellipsoidal intermediates of glucagon were observed inside the small size of lipid bilayer after 4*days, while fibrils grew inside lipid bilayer after 19*days. These results indicate that morphological changes in DMPC/glucagon lipid bilayers are correlated with the evolution of glucagon aggregate state. Particularly, fibril intermediate shows a strong glucagon lipid bilayer interaction. We further investigated the structure and kinetics of glucagon fibril formation inside the DMPC lipid bilayer in a neutral solution using 13C solid-state NMR spectroscopy. ?-Helical structures were observed around Gly4 and Ala19 in the monomeric form, which changed to ?-sheet structures in the fibril form. The fibrillation process can be explained by a two-step autocatalytic reaction mechanism in which the first step is a homogeneous nuclear formation (k1), and the second step is an autocatalytic heterogeneous fibrillation process (k2).
[NMR paper] Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
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Biophys Rev. 2018 May 31;:
Authors: Martial B, Lefèvre T, Auger M
Abstract
It is well established that amyloid proteins play a primary role in neurodegenerative diseases. Alzheimer's, Parkinson's, type II diabetes, and Creutzfeldt-Jakob's...
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[NMR paper] Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by (19)F-NMR observation of 4-fluorophenylalanine.
Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by (19)F-NMR observation of 4-fluorophenylalanine.
Related Articles Solvent-accessibility of discrete residue positions in the polypeptide hormone glucagon by (19)F-NMR observation of 4-fluorophenylalanine.
J Biomol NMR. 2017 May 15;:
Authors: Hou Y, Hu W, Li X, Skinner JJ, Liu D, Wüthrich K
Abstract
The amino acid 4-fluoro-L-phenylalanine (4F-Phe) was introduced at the positions of Phe6 and Phe22 in the 29-residue polypeptide hormone...
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05-17-2017 12:46 PM
[NMR paper] Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Phys Chem Chem Phys. 2013 Oct 21;15(39):16956-64
Authors: Itoh-Watanabe H, Kamihira-Ishijima M,...
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[NMR paper] Probing the Interaction of Arg9Cys Mutated Phospholamban with Phospholipid Bilayers by Solid-state NMR Spectroscopy.
Probing the Interaction of Arg9Cys Mutated Phospholamban with Phospholipid Bilayers by Solid-state NMR Spectroscopy.
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Biochim Biophys Acta. 2013 Jul 9;
Authors: Yu X, Lorigan GA
Abstract
Phospholamban (PLB) is a 52 amino acid integral membrane protein that interacts with the sarcoplasmic reticulum Ca(2+) ATPase (SERCA) and helps to regulate Ca(2+) flow. PLB inhibits SERCA impairing Ca(2+) translocation. The...
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[NMR paper] Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
Langmuir. 2012 Dec 11;28(49):17071-8
Authors: Wang T, Widanapathirana L, Zhao Y, Hong M
Abstract
Macrocycles made of cholate building blocks were previously found to...
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[NMR paper] NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric h
NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer.
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FEBS Lett. 2002 Mar 27;515(1-3):165-70
Authors: Chang X, Keller D, O'Donoghue SI, Led JJ
Nuclear magnetic resonance (NMR) spectroscopy reveals that higher-order aggregates of glucagon-like peptide-1-(7-36)-amide (GLP-1) in pure water at pH 2.5 are disrupted by 35% 2,2,2-trifluoroethanol (TFE), and form a stable and highly symmetric...
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[NMR paper] Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and
Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states.
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Biochemistry. 2001 Nov 6;40(44):13188-200
Authors: Neidigh JW, Fesinmeyer RM, Prickett KS, Andersen NH
Exendin-4, a 39 amino acid peptide originally isolated from the oral secretions of the lizard Heloderma suspectum, has been shown to share certain activities with glucagon-like-peptide-1 (GLP-1), a 30...
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Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Biochemistry. 2010 Aug 30;
Authors: Kijac A, Shih AY, Nieuwkoop AJ, Schulten K, Sligar SG, Rienstra CM
Nanodiscs are an example of discoidal nanoscale lipid/protein particles that have been extremely useful for the biochemical and biophysical characterization of membrane proteins. They are discoidal lipid bilayer fragments encircled and stabilized by two amphipathic helical...
31P and 13C solid-state NMR analysis of morphological changes of phospholipid bilayers containing glucagon during fibril formation of glucagon under neutral condition.
Linear Mode
